Purification and characterization of a β-galactosidase fromSclerotinia sclerotiorum [PDF]
FEMS Microbiology Letters, 1992 Sclerotinia sclerotiorum secretes β-galactosidase, giving very low activity when cultivated in a medium with glucose as the carbon source. This production is greatly enhanced during growth on different pectin related polysaccharides. An extracellular β-galactosidase was purified 26-fold by ammonium sulfate precipitation, gel filtration and ion exchange
Georges Freyssinet +2 more
openaire +2 more sources
The occurrence of β-galactosidase and β-phosphogalactosidase inLactobacillus caseistrains [PDF]
FEMS Microbiology Letters, 1984 Several strains of Lactobacillus casei of different origins were compared and it was observed that lactose metabolism varied from one strain to the other. Certain strains contained a β-galactosidase, others a β-phosphogalactosidase and others contain both.
M. Casey, F. Hofer, J. Jimeno
openaire +2 more sources
Effect of tunicamycin on α-galactosidase secretion byAspergillus nidulansand the importance ofN-glycosylation [PDF]
FEMS Microbiology Letters, 1994 Aspergillus nidulans released α-galactosidase into the culture medium during the exponential growth on either lactose or galactose as the only carbon source. This enzyme is a glycoprotein. Its treatment with endoglycosidases produces a reduction in its molecular mass but the resulting enzyme conserved some of their carbohydrate components in addition ...
Fernando Laborda +2 more
openaire +2 more sources
Immobilized preparation of cold-adapted and halotolerant Antarctic β-galactosidase as a highly stable catalyst in lactose hydrolysis [PDF]
FEMS Microbiology Ecology, 2007 A cold-active beta-galactosidase of Antarctic marine bacterium Pseudoalteromonas sp. 22b was synthesized by an Escherichia coli transformant harboring its gene and immobilized on glutaraldehyde-treated chitosan beads. Unlike the soluble enzyme the immobilized preparation was not inhibited by glucose, its apparent optimum temperature for activity was 10
Józef Kur +6 more
openaire +3 more sources
Thermostable α-galactosidase fromThermotoga neapolitana: cloning, sequencing and expression [PDF]
FEMS Microbiology Letters, 1998 A gene encoding a thermostable alpha-galactosidase from the hyperthermophile Thermotoga neapolitana was cloned and sequenced. Sequence analysis showed that the 552-amino acid protein is similar to Escherichia coli Raf type alpha-galactosidase and belongs to Family 36 of the glycosyl hydrolases. Recombinant alpha-galactosidase expressed in E. coli has a
Bruce M. Chassy +3 more
openaire +3 more sources
Yersinia pestis lacZexpresses a β-galactosidase with low enzymatic activity [PDF]
FEMS Microbiology Letters, 2006 Although very little, if any, beta-galactosidase activity is detected in Yersinia pestis by a standard Miller assay, we found that Y. pestis KIM6+ cells formed blue colonies on plates containing 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). Searches of the Y.
Alexander G. Bobrov, Robert D. Perry
openaire +3 more sources
Purification and molecular properties of an α-galactosidase synthesized and secreted byAspergillus nidulans [PDF]
FEMS Microbiology Letters, 1993 alpha-Galactosidases from mycelial extract and culture filtrate of Aspergillus nidulans have been purified to homogeneity and utilised to obtain polyclonal antibodies anti-alpha-galactosidase. The enzymatic characteristics and the cross reactivity of the antibodies suggest that alpha-galactosidases isolated from the two sources were the same enzyme ...
A.M. Pedregosa +3 more
openaire +3 more sources
Transcriptional analysis of the β-galactosidase gene (pbg) inClostridium perfringens [PDF]
FEMS Microbiology Letters, 1995 The mode of expression of the beta-galactosidase gene (pbg) of Clostridium perfringens was examined. The pbg gene was transcribed on a single 3.7-kb mRNA. The transcript contained a message for ORF54, located upstream of the pbg gene in the chromosome, indicating that ORF54 and the pbg gene comprise one operon (pbg operon). Expression of the pbg operon
Hideo Hayashi +2 more
openaire +3 more sources
Different domains cooperate to target the human ribosomal L7a protein to the nucleus and to the nucleoli. [PDF]
, 1997 The human ribosomal protein L7a is a component of the major ribosomal subunit. We transiently expressed in HeLa cells L7a-β-galactosidase fusion proteins and studied their subcellular localization by indirect immunofluorescence staining with anti-β ...
Giulia RUSSO +2 more
core +1 more source
Production of β-galactosidase from recombinant Saccharomyces cerevisiae grown on lactose [PDF]
, 2004 Improved productivity and costs reduction in fermentation processes may be attained by using flocculating cell cultures. The production of extracellular heterologous β-galactosidase by recombinant flocculating Saccharomyces cerevisiae cells, expressing
Castro, Inês +4 more
core +1 more source